NAT2 (N-acetyltransferase 2 (arylamine N-acetyltransferase))

2009-01-01   Jhon D Ruiz , José AG Agúndez , Carmen Martínez , Elena García-Martín 

Department of Pharmacology, Medical School, University of Extremadura, Badajoz, Spain (JDR, JA, CM); Department of Biochemistry & Molecular biology & Genetics, School of Biological Sciences, Badajoz, Spain (EGM)

Identity

HGNC
LOCATION
8p22
IMAGE
Atlas Image
LEGEND
Picture from Genetics Home Reference; January 2009.
LOCUSID
ALIAS
AAC2,NAT-2,PNAT

DNA/RNA

Atlas Image

Transcription

The human NAT2 gene has two exons but the coding region, spanning 870 bp is located in exon 2. Functionally active NAT2 enzyme can be obtained after transient heterologous transfection of the open reading frame only, indicating that exon 1 is not necessary to obtain functional enzyme.

Pseudogene

In humans the NAT locus has a pseudogene designated as NATP.

Proteins

Note

NAT enzymes have been identified in several vertebrate and microorganism species. NAT2 proteins differ among species. However, common features include an 83 amino acid N-terminal domain containing five alpha-helices and a short beta-strand; a second domain consisting of nine beta-strands and two short helices; and a third alpha/beta lid domain with four beta-strands and an alpha-helix.

Expression

NAT2 has a restricted expression profile with the highest levels of protein and mRNA being detected in the liver, small intestine and colon. The transcription start site for human NAT2 has been recently localised between 30 and 101 bp upstream of the non-coding exon, with the most frequent TSS located at position -64 relative to exon 1. The region containing the NAT2 transcription start site shares an 85% sequence homology to the region of human NAT1 containing the major transcription start site for NAT1. The functional elements of the NAT2 promoter sequence have not been characterised to date. In addtion the promoter sequence appears to be highly polymorphic.

Localisation

Arylamine N-acetyltransferase 2 is a cytosolic enzyme.

Function

NAT2 is a phase II enzyme that participates in the metabolism of numerous primary arylamines and hydrazine drugs and carcinogens. In addition to their N-acetylation catalytic activity, NAT enzymes have also O-acetylation activity towards N-hydroxyarylamines.

Homology

NAT1 and NAT2 share 87% nucleotide homology in the coding region, whereas NAT1 and NAT2 proteins share 81% amino-acid sequence identity.

Mutations

Note

Seven major single nucleotide polymorphisms that occur isolated or combined have been described in the NAT2 gene. These affect the positions 191, 282, 341, 481, 590, 803 and 857. In addition, rare SNPs affecting the positions 111, 190, 364, 411, 434, 499, 795, 845 and 859 have been described although their frequencies are unknown. For details on NAT2 SNPs and haplotypes, see http://louisville.edu/medschool/pharmacology/Human.NAT2.pdf. Critical gene variants leading to slow acetylation capacity contains mutations at positions 191, 341, 590 or 857. Since some genotypes can be due to the presence of different combinations of haplotypes leading to ambiguous phenotype prediction, haplotype reconstruction is often necessary to clarify ambiguous genotype data.
Atlas Image

Implicated in

Note
Determination of the NAT2 genotype or phenotype has been proposed to predict adverse reactions in patients with tuberculosis receiving isoniazid, prior to the concomitant administration of drug combinations such as procainamide-phenytoin or doxycyline-rifampin. In addition, several human diseases have been related to NAT2 polymorphism. There are described below.
Entity name
Brain cancer
Prognosis
Preliminary findings argue for association of a trend towards higher risk in individuals classified as NAT2 homozygous rapid acetylators in patients with astrocytoma or meningioma.
Entity name
Lung cancer
Prognosis
Several studies based on an initial hypothesis that slow acetylation may increase the risk of developing lung cancer have been conducted. This hypothesis has been reinforced by studies indicating that slow acetylation, especially if it is associated to defect genotypes for other phase II enzymes, may confer increased susceptibility to the formation of adducts. Several studies have concluded that the NAT2 slow acetylation genotype causes a marginally increased risk of developing lung cancer. In spite of these findings, present evidence suggests that the NAT2 polymorphism alone does not constitute a relevant risk factor for lung cancer. However this polymorphism may reinforce the effect of other genetic and/or environmental factors.
Entity name
Liver cancer
Prognosis
A role for xenobiotic-metabolising enzymes in liver carcinogenesis is to be expected among patients with environmentally-related liver cancer since, besides viral hepatitis, liver cancer may be related to environmental substances. The findings obtained in patients with primary liver cancer not related to viral hepatitis are consistent and indicate a minor, but relevant, association of the slow NAT2 acetylation status and predisposition to liver cancer.
Entity name
Colorectal cancer
Prognosis
The hypothesis that acetylator status may predispose to a determined cancer risk is based on a differential effect of N-acetylation as a potential detoxification step and O-acetylation as a potential carcinogen-activation step. In the case of colorectal cancer it was hypothesized that O-acetylation is more relevant that N-acetylation, and therefore the rapid acetylation genotype is the putative risk status associated with colorectal cancer. Sufficient evidence is available to rule out a relevant association of NAT genotypes alone with colorectal cancer risk. However, the putative interaction of meat consumption and the NAT2 genotype deserves particular attention.
Entity name
Bladder cancer
Prognosis
Despite the large number of studies and meta-analyses performed in several human populations, current evidence is not sufficient to confirm unambiguously an association of NAT2 polymorphism to overall bladder cancer risk. A general association of the slow acetylation status with bladder cancer risk has not been fully confirmed, although meta-analyses have obtained positive findings for a modest association of the slow NAT2 acetylation genotype with bladder cancer risk, with odds ratio values between 1.3 and 1.5. Furthermore, the biological basis for the putative association is uncertain. In diverse independent studies, mutagenicity in urine was tested in individuals exposed to urban pollution, smoking, red meat intake or textile dyes. In all cases, no higher mutagenicity in slow NAT2 acetylators could be established when compared to these or rapid acetylators, and in fact among individuals exposed to urban pollution, rapid acetylators showed a higher mutagenicity in urine than slow acetylators. In a study investigating the influence of NAT genotypes in the association between permanent hair dyes and bladder cancer, a significant association of the slow NAT2 acetylation genotype was identified. However these findings could not be replicated in other studies.
Entity name
Breast cancer
Prognosis
After dozens of studies involving several thousands of breast cancer patients, as well as meta-analyses, today it is obvious that no major association of NAT2 polymorphism and breast cancer risk exists.
Entity name
Head and neck cancer
Prognosis
Since chemical compounds present in tobacco are inactivated by phase II enzymes, it has been proposed that head and neck cancer risk could be modified by NAT genotypes. However, overall findings indicate that no relevant association between NAT2 polymorphism and head and neck cancer risk is to be expected.
Entity name
Other diseases
Disease
Although a relation of risk may be definitely discarded for systemic lupus erythematosus (SLE), inflammatory bowel disease and endometriosis, more research is needed for rheumatoid arthritis, Parkinsons, Alzheimers, Behçets and periodontal diseases, as current results are inconclusive but suggest a possible relation with NAT2 polymorphism. In diabetes mellitus the possible relation with the rapid phenotype may be due to acquired metabolic changes and more genotyping studies are needed. NAT2 slow metabolizers are more prone to the side effects of polymorphically acetylated drugs, as is the SLE-like syndrome induced by hydralazine and procainamide, the side effects due to sulphasalazine and the skin rash secondary to many sulphonamides.

Bibliography

Pubmed IDLast YearTitleAuthors
186644432008Unraveling ambiguous NAT2 genotyping data.Agúndez JA et al
186804652008N-acetyltransferases: lessons learned from eighty years of research.Agúndez JA et al
186804752008N-acetyltransferases as markers for asthma and allergic/atopic disorders.Batra J et al
16757941991Molecular mechanism of slow acetylation of drugs and carcinogens in humans.Blum M et al
23400911990Human arylamine N-acetyltransferase genes: isolation, chromosomal localization, and functional expression.Blum M et al
186804692008Regulation of arylamine N-acetyltransferases.Butcher NJ et al
28599771985Genetically determined variability in acetylation and oxidation. Therapeutic implications.Clark DW et al
76952651994Possible implications of doxycycline-rifampin interaction for treatment of brucellosis.Colmenero JD et al
5157731979Agranulocytosis during combined procainamide and phenytoin therapy.Crook JE et al
138209681960Genetic control of isoniazid metabolism in man.EVANS DA et al
136975561960The determination of the isoniazid inactivator phenotype.EVANS DA et al
186804682008Interethnic and intraethnic variability of NAT2 single nucleotide polymorphisms.García-Martín E et al
27341091989Nucleotide sequence of an intronless gene for a human arylamine N-acetyltransferase related to polymorphic drug acetylation.Grant DM et al
29249041989Evidence for two closely related isozymes of arylamine N-acetyltransferase in human liver.Grant DM et al
186804662008Structures of human arylamine N-acetyltransferases.Grant DM et al
80813591994Molecular genetics of human polymorphic N-acetyltransferase: enzymatic analysis of 15 recombinant wild-type, mutant, and chimeric NAT2 allozymes.Hein DW et al
186804732008Influence of polymorphic N-acetyltransferases on non-malignant spontaneous disorders and on response to drugs.Ladero JM et al
186804742008Human N-acetyltransferases and drug-induced hepatotoxicity.Makarova SI et al
186804702008Effect of environmental substances on the activity of arylamine N-acetyltransferases.Rodrigues-Lima F et al
186804712008Arylamine N-acetyltransferases in mycobacteria.Sim E et al
108762412000Structure of arylamine N-acetyltransferase reveals a catalytic triad.Sinclair JC et al
186804672008Structure/function evaluations of single nucleotide polymorphisms in human N-acetyltransferase 2.Walraven JM et al
56782191968The mechanism of isoniazid acetylation by human N-acetyltransferase.Weber WW et al
176563652007Structural basis of substrate-binding specificity of human arylamine N-acetyltransferases.Wu H et al

Other Information

Locus ID:

NCBI: 10
MIM: 612182
HGNC: 7646
Ensembl: ENSG00000156006

Variants:

dbSNP: 10
ClinVar: 10
TCGA: ENSG00000156006
COSMIC: NAT2

RNA/Proteins

Gene IDTranscript IDUniprot
ENSG00000156006ENST00000286479P11245
ENSG00000156006ENST00000286479A4Z6T7
ENSG00000156006ENST00000520116E7EWF9

Expression (GTEx)

0
5
10
15
20
25
30
35
40
45
50

Pathways

PathwaySourceExternal ID
Caffeine metabolismKEGGko00232
Drug metabolism - other enzymesKEGGko00983
Caffeine metabolismKEGGhsa00232
Drug metabolism - other enzymesKEGGhsa00983
Metabolic pathwaysKEGGhsa01100
Chemical carcinogenesisKEGGhsa05204
Chemical carcinogenesisKEGGko05204
MetabolismREACTOMER-HSA-1430728
Biological oxidationsREACTOMER-HSA-211859
Phase II conjugationREACTOMER-HSA-156580
AcetylationREACTOMER-HSA-156582

Protein levels (Protein atlas)

Not detected
Low
Medium
High

PharmGKB

Entity IDNameTypeEvidenceAssociationPKPDPMIDs
PA10715sulfamethoxazole / trimethoprimChemicalLabelAnnotationassociated
PA164712505Antivirals for treatment of HIV infections, combinationsChemicalVariantAnnotationassociatedPKPD
PA164712708Drugs For Treatment Of TuberculosisChemicalClinicalAnnotation, VariantAnnotationambiguousPKPD10751073, 11595069, 11915035, 12668988, 16246623, 16677176, 16770646, 17950035, 18023090, 18330759, 18421452, 18713495, 19686464, 19761367, 20392357, 21047300, 21261721, 21753138, 21856096, 22012226, 22020825, 22162992, 22283902, 22506592, 22788240, 22947533, 23190413, 23277397, 23394127, 23875638, 24188272, 24465778, 24637014, 24888881, 26616266, 27340556, 28799976, 29036176, 29781872
PA164749650pyridoxal phosphateChemicalVariantAnnotationnot associatedPKPD16770646
PA164779050sulfapyridineChemicalVariantAnnotationassociatedPK18167504, 19560446, 20040334
PA164784021ethambutolChemicalClinicalAnnotation, VariantAnnotationambiguousPKPD10751073, 11595069, 12668988, 17950035, 18330759, 18421452, 19686464, 19891553, 20392357, 21047300, 21261721, 21753138, 21856096, 22020825, 22506592, 22947533, 23190413, 23875638, 24188272, 26911349, 29036176
PA164925725Toxic liver diseaseDiseaseClinicalAnnotation, VariantAnnotation, VipGeneambiguousPKPD10751073, 11915035, 12668988, 16246623, 16677176, 16770646, 17950035, 18023090, 18330759, 18421452, 18713495, 19761367, 20392357, 21047300, 21261721, 21753138, 21856096, 22012226, 22020825, 22162992, 22283902, 22506592, 22788240, 22947533, 23190413, 23277397, 23394127, 23875638, 24188272, 24465778, 24637014, 24888881, 26616266, 26911349, 27340556, 28799976, 29781872
PA165108622Drug interaction with drugDiseaseClinicalAnnotationassociatedPD
PA165816579CYP2D6*4HaplotypeLabelAnnotationassociated
PA165817016Kidney TransplantationDiseaseVariantAnnotationassociatedPK
PA1658205851,7-dimethylxanthineChemicalVariantAnnotationassociatedPK17011540
PA165949098NAT2*4HaplotypeVipGeneassociated15558239, 18330759, 18421452, 19356010, 19686464, 19891553, 20038957, 20392357, 20602614, 21479500, 21856096, 22506592, 22676187, 23407048, 23875638, 7273597, 11595069
PA166048714PregnancyDiseaseVariantAnnotationnot associatedPD11755554
PA166119041drug-induced liver injuryDiseaseVariantAnnotation, VipGeneambiguousPKPD24888881, 29781872
PA166119201daniquidoneChemicalLiterature, MultilinkAnnotationassociated23912694
PA166120927drug reaction with eosinophilia and systemic symptomsDiseaseVariantAnnotationnot associatedPD29458119
PA166120929severe cutaneous adverse reactionsDiseaseVariantAnnotationassociatedPD11191886
PA166128206dipyroneChemicalClinicalAnnotation, VariantAnnotationassociatedPKPD25241292, 26111152
PA166157267rs776746VariantLabelAnnotationassociated
PA166157540rs1208VariantVipGeneassociated15558239, 18330759, 18421452, 19356010, 19686464, 19891553, 20038957, 20392357, 20602614, 21479500, 21856096, 22506592, 22676187, 23407048, 23875638, 7273597, 11595069
PA166157549rs1041983VariantVipGeneassociated15558239, 18330759, 18421452, 19356010, 19686464, 19891553, 20038957, 20392357, 20602614, 21479500, 21856096, 22506592, 22676187, 23407048, 23875638, 7273597, 11595069
PA166157560rs1495741VariantVipGeneassociated15558239, 18330759, 18421452, 19356010, 19686464, 19891553, 20038957, 20392357, 20602614, 21479500, 21856096, 22506592, 22676187, 23407048, 23875638, 7273597, 11595069
PA166157563rs1799929VariantVipGeneassociated15558239, 18330759, 18421452, 19356010, 19686464, 19891553, 20038957, 20392357, 20602614, 21479500, 21856096, 22506592, 22676187, 23407048, 23875638, 7273597, 11595069
PA166157564rs1799930VariantVipGeneassociated15558239, 18330759, 18421452, 19356010, 19686464, 19891553, 20038957, 20392357, 20602614, 21479500, 21856096, 22506592, 22676187, 23407048, 23875638, 7273597, 11595069
PA166157565rs1799931VariantVipGeneassociated15558239, 18330759, 18421452, 19356010, 19686464, 19891553, 20038957, 20392357, 20602614, 21479500, 21856096, 22506592, 22676187, 23407048, 23875638, 7273597, 11595069
PA166157570rs1801280VariantVipGeneassociated15558239, 18330759, 18421452, 19356010, 19686464, 19891553, 20038957, 20392357, 20602614, 21479500, 21856096, 22506592, 22676187, 23407048, 23875638, 7273597, 11595069
PA166157597rs4271002VariantVipGeneassociated15558239, 18330759, 18421452, 19356010, 19686464, 19891553, 20038957, 20392357, 20602614, 21479500, 21856096, 22506592, 22676187, 23407048, 23875638, 7273597, 11595069
PA166157603rs4646244VariantVipGeneassociated15558239, 18330759, 18421452, 19356010, 19686464, 19891553, 20038957, 20392357, 20602614, 21479500, 21856096, 22506592, 22676187, 23407048, 23875638, 7273597, 11595069
PA166165147solithromycinChemicalVariantAnnotationassociatedPK
PA166176017hydralazine / isosorbide dinitrateChemicalLabelAnnotationassociated
PA166176022isoniazid / pyrazinamide / rifampinChemicalLabelAnnotationassociated
PA166182002amifampridine phosphateChemicalLabelAnnotationassociated
PA166185150amifampridineChemicalLabelAnnotationassociated
PA443227Abortion, SpontaneousDiseaseVariantAnnotationnot associatedPD11755554
PA443250Acquired Immunodeficiency SyndromeDiseaseVariantAnnotationassociatedPD11191886
PA443434Arthritis, RheumatoidDiseaseVariantAnnotationambiguousPD18398952, 24394199
PA443450AsthmaDiseaseClinicalAnnotationassociatedPD20602614
PA443512Urinary Bladder NeoplasmsDiseaseVipGeneassociated
PA443937Drug ToxicityDiseaseClinicalAnnotation, VipGeneassociatedPKPD10751073, 11915035, 12668988, 16246623, 16677176, 16770646, 17950035, 18023090, 18330759, 18421452, 18713495, 19761367, 20392357, 21047300, 21261721, 21753138, 21856096, 22012226, 22020825, 22162992, 22283902, 22506592, 22788240, 22947533, 23190413, 23277397, 23394127, 23875638, 24188272, 24465778, 24637014, 24888881, 26616266, 27340556, 29781872
PA444153FatigueDiseaseVariantAnnotationassociatedPK30520338
PA444435HepatitisDiseaseVariantAnnotationassociatedPKPD11915035
PA444442Hepatitis, ToxicDiseaseClinicalAnnotation, VariantAnnotationambiguousPKPD10751073, 11915035, 12668988, 16246623, 16677176, 16770646, 17950035, 18023090, 18330759, 18421452, 18713495, 19761367, 20392357, 21047300, 21261721, 21753138, 21856096, 22012226, 22020825, 22162992, 22283902, 22506592, 22788240, 22947533, 23190413, 23277397, 23394127, 23875638, 24188272, 24465778, 24637014, 24888881, 26616266, 27340556, 29781872
PA444546HypersensitivityDiseaseVariantAnnotationambiguousPD12043950, 26111152, 8689813
PA444552HypertensionDiseaseClinicalAnnotationassociatedPD1136859, 21781652, 2231320, 24444407, 318493, 5026380
PA444626Insulin ResistanceDiseaseVariantAnnotationassociated
PA444819Lupus erythematosusDiseaseVipGeneassociated
PA444822Lupus Erythematosus, SystemicDiseaseVariantAnnotationassociatedPK16531626
PA445204Ovarian NeoplasmsDiseaseClinicalAnnotationassociatedPD24533712
PA445253ParesthesiaDiseaseVariantAnnotationassociatedPK30520338
PA445355PneumoniaDiseaseVariantAnnotationassociatedPD9923584
PA445425Prostatic NeoplasmsDiseaseClinicalAnnotationassociatedPD20038957
PA445676Skin DiseasesDiseaseVariantAnnotationnot associatedPD29458119
PA445941TuberculosisDiseaseClinicalAnnotation, VariantAnnotationambiguousPKPD10751073, 11595069, 11915035, 12668988, 15855489, 16182272, 16246623, 16531626, 16677176, 16770646, 17950035, 18023090, 18330759, 18421452, 18544910, 18713495, 19686464, 19761367, 19891553, 20392357, 21047300, 21261721, 21479500, 21558457, 21753138, 21856096, 22012226, 22020825, 22162992, 22283902, 22506592, 22788240, 22947533, 23099118, 23190413, 23277397, 23394127, 23875638, 24188272, 24383060, 24465778, 24533708, 24637014, 24888881, 26616266, 26911349, 27340556, 28799976, 29036176, 29781872
PA447230HIVDiseaseVariantAnnotationambiguousPKPD11186133, 12043950, 8689813
PA448497aspirinChemicalClinicalAnnotationassociatedPD20602614
PA448710caffeineChemicalVariantAnnotation, VipGeneambiguousPKPD11755554, 22105431
PA449014cisplatinChemicalClinicalAnnotationassociatedPD24533712
PA449050clonazepamChemicalPathway, VariantAnnotation, VipGeneassociatedPK30520338
PA449165cyclophosphamideChemicalClinicalAnnotationassociatedPD24533712
PA449211dapsoneChemicalVariantAnnotationnot associatedPD29458119
PA449383docetaxelChemicalClinicalAnnotationassociatedPD20038957
PA449441efavirenzChemicalLiterature, MultilinkAnnotationassociated23990572
PA449894hydralazineChemicalClinicalAnnotation, VariantAnnotation, VipGeneambiguousPKPD1136859, 1396201, 17761710, 21781652, 2231320, 24444407, 24702251, 318493, 445966, 5026380, 7284051, 7298112, 7408395, 7438695, 7471604
PA450112isoniazidChemicalClinicalAnnotation, LabelAnnotation, Literature, MultilinkAnnotation, VariantAnnotation, VipGeneambiguousPKPD10751073, 11595069, 11915035, 12668988, 15855489, 16182272, 16246623, 16531626, 16677176, 16770646, 17950035, 18023090, 18330759, 18421452, 18544910, 18713495, 19686464, 19761367, 19891553, 20392357, 21047300, 21261721, 21479500, 21558457, 21753138, 21856096, 22012226, 22020825, 22162992, 22283902, 22506592, 22788240, 22947533, 23099118, 23190413, 23277397, 23394127, 23875638, 24188272, 24383060, 24465778, 24533708, 24637014, 24798717, 24888881, 26616266, 26911349, 27340556, 29036176, 29781872
PA450947phenytoinChemicalClinicalAnnotationassociatedPD
PA451108procainamideChemicalLabelAnnotationassociated
PA451182pyrazinamideChemicalClinicalAnnotation, VariantAnnotationambiguousPKPD11595069, 12668988, 16677176, 17950035, 18330759, 18421452, 19686464, 19891553, 20392357, 21047300, 21261721, 21753138, 21856096, 22020825, 22283902, 22506592, 23099118, 23190413, 23394127, 23875638, 24188272, 26911349, 29036176
PA451250rifampinChemicalClinicalAnnotation, VariantAnnotationambiguousPKPD10751073, 11595069, 12668988, 16246623, 16677176, 17950035, 18330759, 18421452, 19686464, 19891553, 20392357, 21047300, 21261721, 21753138, 21856096, 22020825, 22283902, 22506592, 22788240, 22947533, 23099118, 23190413, 23394127, 23875638, 24188272, 26911349, 29036176
PA451512streptomycinChemicalVariantAnnotationambiguousPKPD10751073, 21753138, 22947533
PA451542sulfamethazineChemicalVariantAnnotationassociatedPK
PA451544sulfamethoxazoleChemicalVariantAnnotation, VipGeneambiguousPKPD11186133, 11191886, 12043950, 8689813, 9923584
PA451547sulfasalazineChemicalLabelAnnotation, VariantAnnotation, VipGeneambiguousPKPD18167504, 18398952, 19560446, 24394199
PA451644thalidomideChemicalClinicalAnnotationassociatedPD20038957
PA451788trimethoprimChemicalVariantAnnotationambiguousPD11191886, 12043950, 8689813, 9923584

References

Pubmed IDYearTitleCitations
209724382010A multi-stage genome-wide association study of bladder cancer identifies multiple susceptibility loci.188
161123012005NAT2 slow acetylation, GSTM1 null genotype, and risk of bladder cancer: results from the Spanish Bladder Cancer Study and meta-analyses.174
117514402001Metabolic gene polymorphism frequencies in control populations.157
199131212009Gene-centric association signals for lipids and apolipoproteins identified via the HumanCVD BeadChip.85
157461602005Constitutional short telomeres are strong genetic susceptibility markers for bladder cancer.83
126689882003Cytochrome P450 2E1 genotype and the susceptibility to antituberculosis drug-induced hepatitis.77
119150352002Polymorphism of the N-acetyltransferase 2 gene as a susceptibility risk factor for antituberculosis drug-induced hepatitis.73
119150352002Polymorphism of the N-acetyltransferase 2 gene as a susceptibility risk factor for antituberculosis drug-induced hepatitis.73
124198322002A pharmacogenetic study to investigate the role of dietary carcinogens in the etiology of colorectal cancer.58
117514432001Combined effects of well-done red meat, smoking, and rapid N-acetyltransferase 2 and CYP1A2 phenotypes in increasing colorectal cancer risk.55

Citation

Jhon D Ruiz ; José AG Agúndez ; Carmen Martínez ; Elena García-Martín

NAT2 (N-acetyltransferase 2 (arylamine N-acetyltransferase))

Atlas Genet Cytogenet Oncol Haematol. 2009-01-01

Online version: http://atlasgeneticsoncology.org/gene/41498/nat2